Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2003-7-9
pubmed:abstractText
PTP1B has been shown to be a negative regulator of the insulin signal transduction in insulin resistant states. Herein we investigated IR/PTP1B interaction and downstream signaling in insulin sensitive tissues of 10 and 28-week-old MSG-insulin resistant rats which represent different stages of insulin resistance. Our results demonstrated that the increase in PTP1B expression and/or association with IR in MSG animals may contribute to the impaired insulin signaling mainly in liver and muscle. Although, adipose tissue of 10-week-old MSG rats showed higher PTP1B expression and IR/PTP1B interaction, they were not sufficient to impair all insulin signaling since IRS-2 phosphorylation and association with PI3-kinase and Akt serine phosphorylation were increased, which may contribute for the increased adiposity of these animals. In 28-week-old-MSG rats there was an increase in IR/PTP1B interaction and reduced insulin signaling in liver, muscle and adipocytes, and a more pronounced insulin resistance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Akt1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Insulin Receptor Substrate Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Irs1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Irs2 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt, http://linkedlifedata.com/resource/pubmed/chemical/Ptpn1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Glutamate, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1369-81
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12850498-Adipose Tissue, pubmed-meshheading:12850498-Aging, pubmed-meshheading:12850498-Animals, pubmed-meshheading:12850498-Animals, Newborn, pubmed-meshheading:12850498-Insulin, pubmed-meshheading:12850498-Insulin Receptor Substrate Proteins, pubmed-meshheading:12850498-Insulin Resistance, pubmed-meshheading:12850498-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:12850498-Liver, pubmed-meshheading:12850498-Male, pubmed-meshheading:12850498-Muscle, Skeletal, pubmed-meshheading:12850498-Phosphatidylinositol 3-Kinases, pubmed-meshheading:12850498-Phosphoproteins, pubmed-meshheading:12850498-Phosphorylation, pubmed-meshheading:12850498-Protein Tyrosine Phosphatase, Non-Receptor Type 1, pubmed-meshheading:12850498-Protein Tyrosine Phosphatases, pubmed-meshheading:12850498-Protein-Serine-Threonine Kinases, pubmed-meshheading:12850498-Proto-Oncogene Proteins, pubmed-meshheading:12850498-Proto-Oncogene Proteins c-akt, pubmed-meshheading:12850498-Rats, pubmed-meshheading:12850498-Rats, Wistar, pubmed-meshheading:12850498-Receptor, Insulin, pubmed-meshheading:12850498-Signal Transduction, pubmed-meshheading:12850498-Sodium Glutamate, pubmed-meshheading:12850498-Tyrosine
pubmed:year
2003
pubmed:articleTitle
Modulation of IR/PTP1B interaction and downstream signaling in insulin sensitive tissues of MSG-rats.
pubmed:affiliation
Departamento de Clínica Médica, Faculdade de Ciências Médicas, Universidade Estadual de Campinas, FCM-UNICAMP, 13081-970 Campinas, SP, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't